Join us for a fascinating conversation with Dr. Subhoja Chakraborty from the University of Central Florida, whose cutting-edge research targets the global challenge of malaria drug resistance. Dr. Chakraborty shares her journey from structure-based drug design during her PhD to her recent collaborative work repurposing human kinase inhibitors as rapid, selective antimalarials against drug-resistant Plasmodium falciparum strains.<h4>In this episode, you'll learn:</h4><ul><li>How structure-guided approaches reveal potential drug targets, including cysteine proteases like falcipain-2, and kinases implicated in malaria's complex life cycle.</li><li>The power of repurposing kinase inhibitors originally developed for cancer and other diseases, focusing on compound 12, which blocks hemozoin formation and protein kinase 6—key steps in parasite survival.</li><li>Lab techniques such as affinity, gel filtration, and size exclusion chromatography for recombinant protein purification—and how troubleshooting is crucial for high-yield, stable complexes.</li><li>Advances in mass spectrometry for characterizing protein interactions, validating drug targets, and mapping molecular pathways pivotal to malaria therapeutics.</li><li>Tips and lessons for new researchers facing the challenges of sample preparation, complex protocols, and working as part of a collaborative team.</li></ul>Dr. Chakraborty’s insights bridge the gap between basic science and translational drug discovery, offering hope for more effective, targeted malaria treatments in a world where resistance to frontline therapies threatens millions.<h4>Referenced Papers:</h4><ul><li>"Plasmodium falciparum protein kinase 6 and hemozoin formation are inhibited by a type II human kinase inhibitor exhibiting antimalarial activity" (Cell Chemical Biology, 2025)</li><li>"New insights of falcipain 2 structure from Plasmodium falciparum 3D7 strain" (BBRC, 2022)</li><li>"Structure-Based Optimization of Protease−Inhibitor Interactions to Enhance Specificity of Human Stefin‑A against Falcipain‑2 from the Plasmodium falciparum 3D7 Strain" (Biochemistry, 2023)</li></ul>If you’re a student, scientist, or simply passionate about advances in infectious disease research, this episode offers actionable insights, inspiring advice, and a front-row seat to innovation in combating malaria.<h3>Video Transcription</h3><h4>From Structural Biology to Drug Discovery: Chromatography and Mass Spectrometry in Malaria Research</h4><h5>Introduction</h5>In this discussion, Subhoja shares insights into her research journey, focusing on malaria drug discovery and the role of modern analytical techniques in biological and biomedical research. The conversation is aimed primarily at undergraduate students and early-career researchers interested in chemistry, biotechnology, and life sciences.<h5>Research Focus: Malaria Drug Discovery and Kinase Targets</h5>Subhoja is currently involved in malaria drug discovery research at the University of Central Florida, where she has been working since beginning her postdoctoral position two years ago. Her earlier PhD research focused on structure-based drug design in malaria, using a combination of in silico approaches, recombinant protein expression, and X-ray crystallography to determine precise three-dimensional structures of target proteins and their inhibitors.This structural perspective provided a foundation for her current work, which centers on drug discovery through compound screening and repurposing. A recent publication from her laboratory explores the use of repurposed mammalian CDK-like kinase inhibitors as potential antimalarial agents. While such kinase inhibitors are well known in cancer and cardiovascular research, their application to malaria targets represents a novel and promising approach.Kinases are attractive drug targets because of their central role in cell signaling and growth pathways. By targeting specific kinases involved in different stages of the malaria parasite life cycle—whether asexual growth, gametocytogenesis, or differentiation—it may be possible to significantly inhibit parasite growth and progression.<h5>Chromatography in Protein Expression and Purification Workflows</h5>Chromatography plays a critical role throughout Subhoja’s research. Her experience spans from basic chromatography techniques during her early training to advanced protein purification workflows using affinity chromatography, gel filtration (size exclusion chromatography), and ion exchange chromatography.Recombinant proteins are routinely purified using affinity resins such as nickel or cobalt, followed by further purification to remove contaminants. Fast Protein Liquid Chromatography (FPLC) enables compact, stepwise purification workflows suitable for producing proteins for in vitro assays.A recurring challenge in this process is the expression of high-molecular-weight proteins, which often accumulate in insoluble fractions or inclusion bodies. Careful selection of expression vectors, host systems, and induction conditions is therefore essential to maximize yield and solubility.<h5>Integrating Size Exclusion Chromatography into the Workflow</h5>Size exclusion chromatography (SEC) is typically used after affinity purification to further improve protein purity. Following elution with imidazole or glutathione, desalting is required to prevent buffer components from interfering with downstream assays. This is often achieved using desalting columns such as G-25 or PD-10.To remove lower-molecular-weight contaminants, finer SEC media—such as Superdex or Sephacryl columns—are employed. Concentration steps using molecular-weight cut-off filters are then applied to obtain the desired protein concentration for functional studies.These iterative purification and troubleshooting steps are a routine part of protein biochemistry and reflect the importance of methodical optimization and careful validation.<h5>The Role of Mass Spectrometry in Biomolecular Characterization</h5>Mass spectrometry is a key analytical tool in Subhoja’s research pipeline, particularly for target identification and validation. In both malaria and cancer research, MS is used alongside chromatography, immunoprecipitation, and pull-down assays to study protein interactions and molecular recognition events.Affinity-based mass spectrometry enables the identification of binding partners and interactors, whether studying proteins, long non-coding RNAs, or protein complexes. Techniques such as native MS, tandem affinity purification, and proximity labeling (e.g., TurboID-based workflows) provide deeper insights into molecular networks and signaling pathways.These approaches are essential for understanding how candidate drug targets function within complex biological systems.<h5>Sample Preparation Challenges in Biological Research</h5>Sample preparation remains one of the most challenging aspects of biological experimentation. Whole-cell lysates contain proteases, nucleases, and other components that can rapidly degrade target molecules. Preventing degradation requires minimizing preparation time, maintaining low temperatures, and using appropriate inhibitor cocktails.Reproducibility is also critical: biological experiments require multiple replicates, and variability is often unavoidable. Careful handling, protocol optimization, and continuous troubleshooting are essential to ensure reliable results, whether preparing samples for chromatography, mass spectrometry, sequencing, or immunoprecipitation.<h5>Advances in Chromatography and MS for Malaria Research</h5>Modern advances in chromatography and mass spectrometry significantly enhance malaria research by enabling precise target identification, quantification, and functional characterization. Drug discovery workflows begin with construct design and recombinant expression, followed by purification and interaction studies.In malaria research, stage-specific parasite biology requires careful extraction and analysis of proteins from different life cycle stages. Tandem affinity MS, immunoprecipitation, and in vivo validation studies help confirm target relevance and therapeutic potential.Recent work on repurposed kinase inhibitors has shown promising results, including inhibition of hemozoin formation—a key detoxification pathway for the malaria parasite—highlighting the potential of such compounds for further development.<h5>Malaria, Drug Resistance, and Global Impact</h5>Malaria remains a major global health burden, with over 600,000 deaths annually and widespread drug resistance complicating treatment. Artemisinin resistance, particularly associated with mutations in the K13 propeller domain, has driven the search for new targets and therapies.During her PhD, Subhoja focused on falcipain-2, a cysteine protease involved in hemoglobin degradation within the parasite. This pathway is critical for parasite survival and has emerged as a promising drug target. Her work revealed that falcipain-2 operates within a larger protein complex responsible for hemoglobin processing and amino acid release.Understanding these molecular mechanisms is essential for developing robust, stage-specific antimalarial strategies.<h5>Advice for Early-Career Researchers</h5>For researchers just starting out, Subhoja emphasizes the importance of hands-on experience. Working directly with cells, lysates, and analytical tools is essential for truly understanding experimental systems. Failure is an inherent part of research, and perseverance is key.Motivation, teamwork, careful sample handling, and thorough preparation all contribute to long-term success. Reading extensively, critically evaluating one’s own work, and appreciating incremental progress are vital aspects of a sustainable research career.Every successful experiment—no matter how small—represents meaningful progress and contributes to the broader goals of science and medicine.<h5>Closing Remarks</h5>The discussion highlights how interdisciplinary approaches combining chromatography, mass spectrometry, structural biology, and biochemistry are driving advances in malaria drug discovery. Through careful experimental design, analytical rigor, and collaborative teamwork, researchers can address complex biological challenges and contribute to global health solutions.<blockquote>This text has been automatically transcribed from a video presentation using AI technology. It may contain inaccuracies and is not guaranteed to be 100% correct.</blockquote><blockquote><h4>Concentrating on Chromatography Podcast</h4>Dive into the frontiers of chromatography, mass spectrometry, and sample preparation with host David Oliva. Each episode features candid conversations with leading researchers, industry innovators, and passionate scientists who are shaping the future of analytical chemistry. From decoding PFAS detection challenges to exploring the latest in AI-assisted liquid chromatography, this show uncovers practical workflows, sustainability breakthroughs, and the real-world impact of separation science. Whether you’re a chromatographer, lab professional, or researcher you'll discover inspiring content!You can find Concentrating on Chromatography Podcast in podcast apps:<ul><li><a target="_blank" rel="noopener noreferrer" href="https://open.spotify.com/show/1wZg67rCjoGju4yhqxI3tL">Spotify</a></li><li><a target="_blank" rel="noopener noreferrer" href="https://podcasts.apple.com/tz/podcast/concentrating-on-chromatography/id1788429185">Apple podcast</a></li><li><a target="_blank" rel="noopener noreferrer" href="https://podscan.fm/podcasts/concentrating-on-chromatography">podscan</a></li></ul>and on <a target="_blank" rel="noopener noreferrer" href="https://www.youtube.com/@ChromatographyTalk/videos">YouTube channel</a></blockquote>

Affinity, Gel Filtration, Size Exclusion Chromatography: Repurposing Kinase Inhibitors for Malaria

In the week of February 9, the following webinars await you in the field of liquid phase and especially HPLC and LC/MS.<blockquote><h4><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinars">👉 DETAILS AND REGISTRATION IN THE WEBINARS SECTION</a></h4>👉 Search and filter in the largest global database with over 5 000 GC, LC, MS and spectroscopy webinars.</blockquote><h5>1. SelectScience: High-Throughput Stability Screening Strategies for Antibody Formulation</h5><ul><li>Tu, 10.2.2026 17:00 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5807">Registration</a></li></ul>Learn how high-throughput DLS/SLS and rapid-screening DSC accelerate stability assessment of high-concentration antibody formulations, enabling faster, data-driven biologics development.<h5>2. Phenomenex: Big Scale, Big Wins – Prep Chromatography Explained</h5><ul><li>We, 11.2.2026 10:00 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5793">Registration</a></li></ul>Learn how to scale analytical methods to preparative HPLC, optimize loading capacity, and understand the limits of preparative columns for pharmaceutical applications.<h5>3. ALS Czech Republic: PFAS in Food &amp; Food Contact Material</h5><ul><li>We, 11.2.2026 15:00 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5816">Registration</a></li></ul>Get a practical overview of PFAS in food and food contact materials, including EU and US regulations, key analytical challenges, and reliable PFAS testing strategies.<h5>4. New Food Magazine: The Science of Next-Gen Ingredients – Fermentation, Formulation and Function</h5><ul><li>We, 11.2.2026 16:00 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5720">Registration</a></li></ul>Explore how fermentation-driven innovation is transforming functional food ingredients and how advanced analytics optimize flavour, functionality, and stability.<h5>5. SCIEX: Accurate Mass Fundamentals – Interpreting and Applying Your Data</h5><ul><li>We, 11.2.2026 19:00 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5772">Registration</a></li></ul>Session 3 focuses on interpreting and applying accurate mass data to confirm compound identity, move beyond basic quantitation, and troubleshoot results for confident reporting.<h5>6. Agilent Technologies: Process Analytical Techniques – Online HPLC for Real-Time Monitoring and Control of Bioprocesses</h5><ul><li>Th, 12.2.2026 06:30 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5834">Registration</a></li></ul>Discover how PAT HPLC enables near-real-time monitoring of critical quality attributes in bioprocessing, with a case study on charge-variant control by cation-exchange chromatography.<h5>7. Thermo Fisher Scientific: Introducing the Orbitrap Excedion Pro Hybrid MS</h5><ul><li>Th, 12.2.2026 11:00 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5889">Registration</a></li></ul>Discover the new Orbitrap Exploris Pro with expanded ETD/EThcD capabilities for confident biopharmaceutical characterization, including intact proteins, PTMs, ADCs, and large biomolecules.<h5>8. Waters Corporation: Planning Your NuGenesis Upgrade – Insights and Best Practices for a Smooth Transition</h5><ul><li>Th, 12.2.2026 19:00 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5833">Registration</a></li></ul>Learn how to plan a successful NuGenesis upgrade, transition to Windows 11, and unlock new capabilities such as dashboards for real-time operational insights.<h5>9. Thermo Fisher Scientific: Comprehensive Analytical Strategies for Peptide Therapeutics and GLP-1 Agonists with Agilent</h5><ul><li>Th, 12.2.2026 19:00 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5814">Registration</a></li></ul>Explore analytical workflows for peptide therapeutics, including method development, peptide mapping, GLP-1 QC, and LC-MS strategies across Agilent platforms.<h5>10. Agilent Technologies: Moving from R&amp;D and Limited QC on a UV-Vis-NIR Instrument to Large-Scale QC Using an Autosampler</h5><ul><li>Th, 12.2.2026 20:00 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/2104">Registration</a></li></ul>This webinar covers practical aspects of adding and using an autosampler to maximize UV-Vis-NIR QC workflows at scale.<h5>11. Agilent Technologies: LC Method Transfer – Hidden Challenges &amp; Absolute Solution</h5><ul><li>Fr, 13.2.2026 06:30 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5787">Registration</a></li></ul>Discover why LC method transfer between legacy and modern systems is challenging, which hidden parameters affect retention and peak shape, and how to achieve robust, reliable results.

Webinars LabRulezLCMS Week 07/2026

Charge detection mass spectrometry (CDMS) allows direct mass determination of individual ions and is increasingly used to study heterogeneous biological samples. This work demonstrates the use of Orbitrap-based CDMS/Direct Mass Technology (DMT) for quantitative analysis of transthyretin (TTR) tetramer samples below 100 kDa, extending CDMS beyond its traditional qualitative role.DMT resolved wild-type and C-terminally modified TTR homotetramers, as well as hybrid tetramers, enabling kinetic analysis of subunit exchange and stability. The approach also quantified thyroxine binding to TTR variants, revealing differences in binding affinity linked to C-terminal modification. By separating overlapping m/z signals through charge measurement, CDMS enables accurate mass and abundance determination, highlighting its potential for quantitative analysis of complex protein systems.<blockquote><h4>The original article</h4><h4><a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.analchem.5c05771">Dissecting Heterogeneous Populations of Protein-Complex Samples Using Direct Mass Technology</a></h4>Robert L. Rider, Jared Hampton, Zhenyu Xi, Carter Lantz, Sangho D. Yun, Weijing Liu, Rosa Viner, Arthur Laganowsky, and David H. Russell*Anal. Chem. 2025, 97, 49, 27057–27063<a target="_blank" rel="noopener noreferrer" href="https://doi.org/10.1021/acs.analchem.5c05771">https://doi.org/10.1021/acs.analchem.5c05771</a><h6>licensed under <a target="_blank" rel="noopener noreferrer" href="https://creativecommons.org/licenses/by/4.0/">CC-BY 4.0</a></h6></blockquote>Selected sections from the article follow. Formats and hyperlinks were adapted from the original.Transthyretin (TTR) is a homotetrameric transport protein that circulates in plasma and cerebrospinal fluid, delivering thyroxine (T4) and retinol-binding protein–vitamin A complexes. <a href="javascript:void(0);">(1)</a> The stability of the TTR tetramer is central to its physiological role because dissociation into monomers can initiate misfolding and amyloid formation, leading to systemic or hereditary transthyretin amyloidosis. <a href="javascript:void(0);">(2)</a> Subunit exchange between wild-type (WT) and variant TTR proteoforms, including disease-associated mutations such as V30M and V122I, have been implicated in amyloid progression by generating hybrid tetramers (tetramers containing WT and mutant subunits) with altered stabilities. <a href="javascript:void(0);">(3,4)</a> Ligand binding, particularly at the two thyroxine-binding sites located at the dimer–dimer interface, can kinetically stabilize the tetramer and modulate amyloidogenicity. <a href="javascript:void(0);">(5,6)</a> Accurate measurement of both subunit exchange kinetics and ligand binding stoichiometry is therefore critical for elucidating the TTR dynamics and stability.Affinity or sequence tags are widely employed in protein expression, purification, or detection. <a href="javascript:void(0);">(7,8)</a> While these tags are often assumed to be inert, their influence on protein structure and dynamics are rarely examined in detail. <a href="javascript:void(0);">(9,10)</a> Protein tags at the N- and C-terminus of TTR have been shown to have differing gas phase stabilities from those of WT-TTR. <a href="javascript:void(0);">(11)</a> The C-terminus is of particular interest because this region participates in the dimer–dimer interface that governs tetramer stability. <a href="javascript:void(0);">(11,12)</a> Characterizing how the C-terminal tag (CT) (-ASGENLFYQ) affects TTR’s solution stability and ligand binding is not only relevant for understanding TTR dynamics but also provides an example of how expression tags can alter protein dynamics. <a href="javascript:void(0);">(13)</a>Native mass spectrometry (nMS) has been invaluable for characterizing protein complexes, <a href="javascript:void(0);">(14)</a> yet conventional nMS often struggles with heterogeneous samples where overlapping charge state distributions and adduct heterogeneity limit resolution and quantitation. <a href="javascript:void(0);">(15)</a> Charge detection mass spectrometry (CDMS) addresses these limitations by independently measuring the charge and m/z of individual ions, enabling the direct determination of molecular mass and abundance. Development of CDMS has largely focused on achieving higher mass resolution <a href="javascript:void(0);">(16)</a> and extending measurements toward assemblies into the GDa range. <a href="javascript:void(0);">(17,18)</a> However, there is untapped utility for CDMS experiments other than mass and proteoform determination. Jordan et al. showed the capability to assess conformational heterogeneity of mAb aggregates using the added charge dimension that CDMS provides. <a href="javascript:void(0);">(19)</a> The current work demonstrates that CDMS can separate proteoforms with overlapping m/z values based on charge and quantify their relative abundances in complex mixtures. While nMS is already a highly quantitative technique, our results establish CDMS as an equally powerful tool for quantitative analysis in heterogeneous systems. <a href="javascript:void(0);">(20,21)</a>Here, we apply Orbitrap-based CDMS/Direct Mass Technology (DMT) using the selective temporal overview of resonant ions (STORI) approach <a href="javascript:void(0);">(22,23)</a> to quantitatively compare WT-TTR and CT-TTR, focusing on two biologically relevant properties: tetramer stability assessed via subunit exchange kinetics and ligand-binding affinity. Conventional nMS cannot fully resolve the overlapping charge states of WT- and CT-TTR or their ligand-bound states. However, DMT can resolve these species by directly measuring the mass (m/z × charge), enabling quantitation of all proteoforms. The data reveal that the CT tag alters tetramer stability and thyroxine-binding affinity, demonstrating the structural sensitivity of TTR to modifications at its C-terminus. More broadly, this work demonstrates the impact that protein tags can have on native protein interactions and highlights the broader utility of quantitative CDMS for probing heterogeneous biological samples.<h4>Experimental Section</h4><h5>Data Collection</h5>All experiments were conducted on a <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/560">Thermo Scientific Q-Exactive UHMR</a> with added DMT capabilities (Bremen, Germany). Before DMT, mass spectra were collected at various resolving powers (6–200k) for each sample, with the instrument parameters reported in the Supporting Information (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acs.analchem.5c05771/suppl_file/ac5c05771_si_001.pdf">Table S1</a>). For DMT experiments, the trapping gas pressure in the HCD cell was reduced to 0.3–0.8 to attenuate the signal intensity to a single ion level, as well as decreasing the UHV pressure to assist ion retention through the entire transient of Orbitrap analysis. We observed no significant difference between mass spectra collected at various HCD cell pressures (Supporting Information, <a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acs.analchem.5c05771/suppl_file/ac5c05771_si_001.pdf">Figure S1</a>). For DMT collection, automated ion control (AIC) and 100% target density were used with 200k resolving power.<h4>Results and Discussion</h4>CDMS has emerged as a powerful tool for analyzing heterogeneous biomolecular samples, enabling accurate, direct mass determination by simultaneously measuring the charge and m/z for individual ions. While CDMS has been widely applied for qualitative analyses, its potential for quantitative and less than MDa applications remains underexplored. <a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.analchem.5c05771#fig1">Figure 1</a>A shows the theoretical mass spectrum of WT-TTR (14+ to 16+) and CT-TTR (15+ to 17+) homotetramers, where the two proteoforms become increasingly resolved as the charge states increase (&lt;3900 m/z). <a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.analchem.5c05771#fig1">Figure 1</a>B zooms in on the 14+ (WT) and 15+ (CT) charge states, highlighting their strong overlap, which prevents accurate deconvolution of the proteoforms by conventional methods. <a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.analchem.5c05771#fig1">Figure 1</a>C displays theoretical distributions for 0, 1, and 2 T4 bound states of both WT- and CT-TTR tetramers, where &lt;3900 m/z has observable separation between all proteoforms. However, for the 14+ and 15+ charge states of WT- and CT-TTR, respectively, the 0 T4- and 1 T4-bound populations overlap (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.analchem.5c05771#fig1">Figure 1</a>D). Furthermore, commonly adducted species (Na+, K+, and Zn2+) observed in experimental spectra broaden these distributions, making it increasingly difficult to distinguish and deconvolute the proteoforms (see <a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acs.analchem.5c05771/suppl_file/ac5c05771_si_001.pdf">Figure S2</a>). Here, we employ Orbitrap-based CDMS/DMT to overcome this m/z overlap to resolve and quantify hybrid tetramer formation and T4 binding.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Anal_Chem_2025_97_49_27057_27063_Figure_1_A_Theoretical_mass_spectra_of_WT_TTR_and_CT_TTR_homotetramers_47232849d9.jpg" alt="Anal. Chem. 2025, 97, 49, 27057–27063: Figure 1. (A) Theoretical mass spectra of WT-TTR and CT-TTR homotetramers. (B) Zoomed-in view of the 14+ WT-TTR and 15+ CT-TTR distributions to show the large overlap of the proteoforms. (C) Theoretical mass spectra of WT-TTR and CT-TTR homotetramers with thyroxine (T4) binding. (D) Zoomed-in view of the 14+ WT-TTR and 15+ CT-TTR distributions where the 0 and 1 T4 have overlapping distributions. These theoretical distributions do not contain any commonly adducted species (Na+, K+, Zn2+), which broaden the distributions and create more overlap even for the proteoforms in the range 3300–3900 m/z (see Figure S2)." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Anal_Chem_2025_97_49_27057_27063_Figure_1_A_Theoretical_mass_spectra_of_WT_TTR_and_CT_TTR_homotetramers_47232849d9.jpg 187w," sizes="100vw" width="1417" height="1182"><h5>Thyroxine Binding to TTR Homotetramers</h5>Thyroxine is the less active form of a thyroid hormone important for metabolism that binds to TTR for transport throughout plasma and cerebral spinal fluid. <a href="javascript:void(0);">(31)</a> Turnover of T4 into T3 (active) occurs after dissociation, where it can then modulate gene expression via binding to nuclear receptors. <a href="javascript:void(0);">(32)</a> The TTR tetramer gains substantial stability as it binds up to 2 T4 at the tetramer interface, decreasing tetramer dissociation and SUE. <a href="javascript:void(0);">(33)</a> This has been shown previously to decrease the amyloidogenic rate of TTR, which led to tafamidis (similar in structure to T4) to be designed and is currently the only drug that is approved for clinical treatment of TTR amyloidosis. <a href="javascript:void(0);">(34)</a> Measuring the difference in binding affinity between TTR proteoforms may provide insight into regions of TTR or TTR intermolecular/intramolecular interactions that are important for binding of small molecules such as tafamidis and T4.DMT was further applied to quantify T4 binding to WT- and CT-TTR homotetramers, highlighting the technique’s utility in probing protein–ligand interactions. <a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.analchem.5c05771#fig3">Figure 3</a>A shows a representative mass spectrum of TTR homotetramers in the presence of T4. While ligand-bound species can be observed, homotetramers cannot be confidently resolved across the entire 3000–5000 m/z range. By leveraging the charge-resolving capabilities of DMT, we achieve separation of the homotetramers (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.analchem.5c05771#fig3">Figure 3</a>B,C) and the 0, 1, and 2 ligand-bound states. The 2D plot clearly shows the gain in resolution achieved when charge is simultaneously measured with m/z by separating the 14+ and 15+ charge states for WT and CT, respectively, in the range 3900–4200 m/z. Additionally, using ion mobility does not provide the same kind of 2D resolution due to the similarity in arrival times for the homotetramer proteoforms, as evidenced by <a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acs.analchem.5c05771/suppl_file/ac5c05771_si_001.pdf">Figures S4 and S5</a> (see the Supporting Information). These data provide evidence that when ion mobility is able to separate out species that overlap in m/z yet differ in mobility, CDMS could be an alternative or used complementarily since the species likely also differ in charge.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Anal_Chem_2025_97_49_27057_27063_Figure_3_A_Mass_spectra_of_WT_TTR_and_CT_TTR_homotetramers_with_thyroxine_binding_61b1e98a94.jpg" alt="Anal. Chem. 2025, 97, 49, 27057–27063: Figure 3. (A) Mass spectra of WT-TTR and CT-TTR homotetramers with thyroxine binding. Ligand binding can be resolved, but homotetramers cannot be confidently identified. Charge states labeled are for WT; CT is always one charge state higher at the same m/z range. (B) DMT heatmap resolving WT-TTR and CT-TTR homotetramers with the additional measurement of charge. (C) Deconvoluted mass spectrum from DMT analysis. Both homotetramers and their ligand binding are resolved, and fit for analysis is shown in red. (D) Mole fraction of each homotetramer and their thyroxine binding species. Error bars represent the standard deviation of replicates (n = 3). The significance for each ligand state is in respect to the left adjacent state. *p &lt; 0.05." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Anal_Chem_2025_97_49_27057_27063_Figure_3_A_Mass_spectra_of_WT_TTR_and_CT_TTR_homotetramers_with_thyroxine_binding_61b1e98a94.jpg 181w," sizes="100vw" width="1266" height="1094"><h4>Conclusion</h4>This work demonstrates that quantitatively, Orbitrap-based CDMS/DMT can determine differences in protein-complex stability and ligand binding. By directly comparing WT- with CT-TTR, we show that the CT tag accelerates tetramer dissociation while enhancing T4 binding affinity. These results indicate that the C-terminus, located at the dimer–dimer interface, plays a more significant role in TTR stability and ligand recognition than previously appreciated. <a href="javascript:void(0);">(12)</a> Even the addition of a short peptide sequence perturbs noncovalent interactions at the interface, likely altering solvent accessibility, and the dynamics of the thyroxine binding channel. <a href="javascript:void(0);">(37,54)</a> Such findings underscore the importance of evaluating how seemingly minor sequence modifications, such as affinity tags, can influence fundamental biophysical properties.Beyond TTR, this work positions quantitative CDMS as a broadly applicable strategy for analyzing heterogeneous protein systems, where charge domain separation overcomes the resolution limits of m/z domain measurements in traditional nMS experiments. While much of the field has emphasized extending CDMS to ultrahigh masses and maximal resolution, <a href="javascript:void(0);">(16,18)</a> our results highlight the underexplored potential of applying the method in the 1000–10,000 m/z range common to nMS experiments. This capability is directly relevant to heterogeneous membrane protein complexes, which often display broad distributions of oligomeric states, PTMs, lipid, and ligand adducts that complicate spectra. <a href="javascript:void(0);">(48,55)</a> Similarly, mAbs can oligomerize and exhibit mass heterogeneity from variable glycosylation, affecting pharmacokinetics, effector function, and stability. <a href="javascript:void(0);">(19)</a> CDMS may resolve and quantify such proteoforms in a single experiment without the need for charge reduction or chemical derivatization. <a href="javascript:void(0);">(48,56,57)</a>

Dissecting Heterogeneous Populations of Protein-Complex Samples Using Direct Mass Technology

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Organomation, founded in 1959, designs and manufactures high-quality nitrogen evaporators and extraction systems. Known for innovation and durability, their lab instruments are used globally for efficient sample preparation with strong customer support.

Organomation

Technology Networks

GERSTEL

Phenomenex

SelectScience

C&EN

Shimadzu Corporation

Evosep Biosystems

Tangential flow filtration (TFF), also known as cross-flow filtration, is a rapid and efficient method for the separation and purification of biomolecules.
TFF can be used to concentrate sample solutions ranging in volumes from 10 mL to thousands of liters. It can also be used to fractionate large from small biomolecules, harvest cell suspensions and clarify fermentation broths and cell lysates.
Another major usage of TFF is to perform a process called diafiltration, a technique that uses ultrafiltration membranes to completely remove, replace or lower the concentration of salts or solvents from solutions containing proteins, peptides, nucleic acids and other biomolecules.
This webinar will explore the applications of diafiltration across immunology, protein chemistry, molecular biology, biochemistry and biotechnology.
Attend this webinar to learn:
<ul>
<li>How to optimize laboratory-scale protein purifications</li>
<li>About tangential flow filtration techniques and ultrafiltration membrane selection</li>
<li>How to operate both continuous and discontinuous diafiltration methods</li>
</ul>
Presenter: Richard Pearce (Independent Consultant)

Technology Networks: Simplified Diafiltration for Protein Purification

Simplified Diafiltration for Protein Purification

This webinar will explore the applications of diafiltration across immunology, protein chemistry, molecular biology, biochemistry and biotechnology.

The field of synthetic biology revolves around the design-build-test-learn (DBTL) cycle, where biological components are adjusted in multiple iterations. Automation allows synthetic biologists to spend less time pipetting liquids and devote more time understanding the science and finding creative solutions to problems.
By combining automation for sample preparation with rapid separation methods we provide a phenotyping workflow suited to the needs of the synthetic biology community.
Attend this webinar to discover:
<ul>
<li>Automation solutions for synthetic biology applications</li>
<li>Rapid separation method workflows</li>
<li>How to improve confidence in annotation using ion mobility</li>
</ul>
<blockquote>
Presenter: Dr. Tessa Moses (Metabolomics Specialist and Facility Manager of EdinOmics, Center for Engineering Biology, The University of Edinburgh)
</blockquote>

Technology Networks: An Automated Workflow for Untargeted Metabolomics of Complex Biological Samples

An Automated Workflow for Untargeted Metabolomics of Complex Biological Samples

By combining automation for sample preparation with rapid separation methods we provide a phenotyping workflow for the synthetic biology community.

An Automated Workflow for Untargeted Metabolomics

Unleash the power of DIA and enable the exploration of complex biological systems with unprecedented depth and precision for large-scale quantitative protein analysis combined with short methods on the Evosep One.
<h3>Global proteomics with Evosep and DIA-PASEF</h3>
Recent progress in liquid chromatography and mass spectrometry, as well as sample preparation and search algorithms for spectra deconvolution and identification, plays an important role in bringing proteomics to the forefront of drug discovery and development. Nanoflow liquid chromatography coupled to tandem mass spectrometry is one of the most essential elements in a proteomics workflow. The four dimensional ion detection achieved with the latest generation of Bruker’s trapped ion mobility spectrometers led to superior speed and sensitivity. Evosep One liquid chromatography platform offers speed and robustness while maintaining, even exceeding previously achieved performance level with high-performing nano LC systems. We share here some results only possible with this combination of LC-MS and dia-PASEF.
<blockquote>
Presenter: Anh Reynolds (Scientist, Bristol Myers Squibb)
</blockquote>
<h3>Extending sensitivity limits with Evosep and Slice-PASEF</h3>
Sensitivity improvements in LC-MS proteomics have recently led to exciting new applications, such as comprehensive proteomic profiling of single cells or 2-dimensional proteomics of tissue slices. In this talk, I will describe Slice-PASEF, a new acquisition technology for timsTOF instruments, which, in combination with the DIA-NN data analysis software, provides a fold-change signal boost. When paired with the Evosep system, Slice-PASEF allows to achieve high sensitivity in robust high-throughput workflows, paving a way for accessible sensitive proteomics on a large scale.
<blockquote>
Presenter: Vladim Demichev (Group Leader, Quantitative ProteomicS, Charité – Universitätsmedizin Berlin)
</blockquote>

Pixabay/sethink: Revolutionizing proteomics with Evosep-DIA

Revolutionizing proteomics with Evosep-DIA

Global proteomics with Evosep and DIA-PASEF & Extending sensitivity limits with Evosep and Slice-PASEF.

Join this webinar to learn how to simplify, speed-up, and standardize your proteomics sample preparation for LC-MS.
The PreOmics team will introduce the PreOmics easy-to-use iST technology. This fast 3-step workflow is designed to be a great support for both those new to proteomics and experts alike. The all-in-one iST kits are compatible with a variety of starting materials, including mammalian and plant samples, different types of tissue and cells, as well as various biological fluids in label-free and chemical labelling applications.The protocols promise an incredibly fast processing time (&lt;2.5 hours) and are easily applicable without compromising sample quality or proteomic depth. Furthermore, iST can be fully automated to further increase standardization, reproducibility, and throughput.
The speakers will also introduce PreON, a fully automated sample preparation platform, as well as different levels of automation for established liquid handling platforms. The varying applications for the iST technology ranging from global proteomics to pre-clinical studies will also be discussed.
<h5>Key learning objectives</h5>
<ul>
<li>Discover best practices for proteomics sample preparation with solutions for new users and proteomics experts alike</li>
<li>Learn more about fast, easy, and reliable sample preparation protocols for LC-MS-based proteomics</li>
<li>Explore automation, standardization, and upscaling of proteomics sample preparation</li>
<li>Learn more about the applications of iST sample preparation kits and solutions in global proteomics as well as pre-clinical research</li>
</ul>
<h5>Who should attend?</h5>
<ul>
<li>Users working with proteomics sample preparation for LC-MS:</li>
<li>Researchers, scientists, principal investigators, group leaders and department heads, lab assistants from biotech/pharma industry, CROs, university hospitals as well as academia</li>
<li>Biomedical and clinical scientists in translational and pre-clinical research</li>
<li>Application scientists and technical support</li>
<li>Distributors of sample preparation systems for LC-MS</li>
<li>Scientists looking for a straightforward approach to start with proteomics</li>
</ul>
<blockquote>
Presenter: Dr. Ingrid Albrecht-Walz (PreOmics GmbH)
</blockquote>
<blockquote>
Dr. Ingrid Albrecht-Walz joined PreOmics in 2022 as Product Manager for Kits &amp; Reagents. She received her Ph.D. in Biology from the University of Munich, Germany, working on the interaction of different viruses. For the past 10 years, Dr. Albrecht-Walz has worked in the field of in vitro diagnostics of infectious diseases. Since proteomics is a highly promising tool for preclinical and diagnostic applications, Dr. Albrecht-Walz decided in 2022 to follow this opportunity at PreOmics.
</blockquote>
<blockquote>
Presenter: Dr. Vincenzo Romaniello (PreOmics GmbH)
</blockquote>
<blockquote>
Dr. Vincenzo Romaniello joined PreOmics in 2021 as Product Manager for Automation Systems. He received his Ph.D. in molecular physiology from the University of Göttingen, Germany. During the past 5 years, Dr. Romaniello has worked in both technical and application support roles for automated sample preparation workflows with major biotech and human diagnostics scientific suppliers. As a result, he has experience in PreOmics automation solutions, and Tecan and Eppendorf systems.
</blockquote>
<blockquote>
Presenter: Dr. Zuzana Demianova (PreOmics GmbH)
</blockquote>
<blockquote>
Dr. Demianova joined PreOmics in 2021 as a Market Development Manager BioPharma and scientific advisor. Assessing proceedings and challenges in the pharma and biopharma field Dr. Demianova introduces PreOmics’ solutions in customer workflows to enable scientific discovery. She thereby partakes also in the development and market introduction of new products as well as optimization and application of established solutions. Prior to PreOmics, Dr. Demianova was application support specialist at Sciex, concentrating on customer support and training. Later on, she was promoted to a global leader in proteomics, which finally led up to her new role as a biopharma application scientist with a focus on “-omics” and biopharma applications using CE and LC-MS technologies.
</blockquote>
<blockquote>
Presenter: Blake Forman (SelectScience)
</blockquote>
<blockquote>
Blake studied chemistry at the University of Surrey, UK, and further went on to study a master’s in chemistry at the University of Southampton, UK. Blake has previously worked in the Medicines and Healthcare Products Regulatory Agency (MHRA) lab at LGC and as a technical sales specialist for Waters. As a member of the Editorial team, he now plays an integral role in shaping the content on SelectScience.
</blockquote>

SelectScience: Next generation solutions for proteomics sample preparation

Next generation solutions for proteomics sample preparation

Join this webinar to learn how to simplify, speed-up, and standardize your proteomics sample preparation for LC-MS.

Targeted workflows are particularly interesting for identifying established biomarkers in various applications. The focus on these workflows, coupled with technological advancements, is continually expanding the boundaries of high-throughput targeted analysis.
<h3>Next Generation of absolute protein Quantitation in Biological Matrixes; higher multiplexicity while faster, robust and sensitive</h3>
<ul>
<li>Presenter: Dr. Christoph Borchers (Mcgill university)</li>
</ul>
The accurate and rapid determination of protein concentrations using multiplexed multiple reaction monitoring (MRM) with isotope-labeled internal standards has the potential to revolutionize biochemistry and medical sciences. The combination of an Evosep One LC with an Agilent QQQ6495C allows a several-fold reduction of analysis time while maintaining high multiplexicity. As an example, we show the use of a multi-protein method for the absolute quantitation of 270 proteins, combined with metabolomics and Artificial Intelligence (AI), to analyze the plasma of a COVID cohort for prediction of survival. Moreover, optimization of the Evosep/6495C combination allowed adaptation of the 270-protein MRM method to a 24-minute gradient, thus doubling the throughput compared to before.
<h3>Development of a LC-MS/MS Method for Measurement of Fusion Sarcoma Proteins in Plasma</h3>
<ul>
<li>Presenter: Phd. AnThony Maus (Clinical Mass Spec. Development Laboratory, Mayo Clinic)</li>
</ul>
Sarcoma is general term for a group of over 70 cancers that are classified using genomic techniques to identify characteristic gene fusions in tumor tissues. However, this technique requires relatively invasive biopsies and is not conducive to monitoring disease progression or response to treatment. Measurements of fusion protein biomarkers in plasma would overcome these limitations. We sought to develop an LC-MS/MS method capable of performing these measurements by conducting discovery experiments on cell lines with an EvoSep coupled to an Exploris 480 mass spectrometer. Using these data, we developed a targeted method and performed measurements in plasma samples.

Targeted Workflows

Targeted workflows are particularly interesting for identifying established biomarkers in various applications.

Targeted LC/MS Workflows

Learn how to automate your SPE procedures with the LCTech FREESTYLE™ system for various sample types.
Presenter: Fred Foster (Applications Scientist)

GERSTEL: Automation of Solid Phase Extraction Procedures using a Novel Robotic Automation Platform

Automation of Solid Phase Extraction Procedures using a Novel Robotic Automation Platform

Learn how to automate your SPE procedures with the LCTech FREESTYLE™ system for various sample types.

Automation of Solid Phase Extraction - Automation Platform

Solid phase extraction (SPE) is an effective technique for cleaning up and concentrating samples prior to high performance liquid chromatography (HPLC) or gas chromatography (GC) analysis. The technique offers targeted selectivity for analytes of interest. SPE is versatile for a wide range of sample volumes, can be easily automated for high-throughput, and is performed by following quick and simple methods (condition, equilibrate, load, wash, and elute). In this webinar, learn more about an effective sample cleanup method for steroid analysis that targets 19 analytes utilizing a Polymeric Reversed Phase Strata™-X 96-well plate.
Mackenzie Freige, a Clinical Application Scientist at Phenomenex, will explain the foundation of SPE and offer method development insight to a frequently tested clinical application.
<h5>Key learning objectives</h5>
<ul>
<li>Understand the fundamentals of solid phase extraction (SPE)</li>
<li>Discover the common difficulties of steroid analysis</li>
<li>Learn tips for approaching SPE method development</li>
<li>Explore a review of SPE data</li>
</ul>
<h5>Who should attend?</h5>
<ul>
<li>Scientists working in the field of clinical, forensics and/or toxicology.</li>
<li>Scientists looking to improve their sample preparation techniques.</li>
<li>Scientists who want to learn more about steroids.</li>
</ul>
<h5>Certificate of attendance</h5>
All webinar participants can request a certificate of attendance, including a learning outcomes summary, for continuing education purposes.
<blockquote>
Presenter: Mackenzie Freige (Phenomenex)
</blockquote>
<blockquote>
Mackenzie Freige received a Bachelor of Science degree in Life Sciences from Kansas State University and a Bachelor of Arts degree in Chemistry from Wichita State University, USA. She has six years’ experience in LC-MS/MS, GC-MS, and sample preparation. She has previously worked in toxicology, environmental chemistry, food science industries, and the pharmaceutical industry.
</blockquote>
<blockquote>
She joined Phenomenex in 2021 as an Application Scientist, specializing in developing applications for clinical research. She has experience in method development and instrumentation, which she uses to help customers solve problems regarding sample preparation, HPLC, and MS methods.
</blockquote>
<blockquote>
Presenter: Jemima Arnold (Editorial Team, SelectScience)
</blockquote>
<blockquote>
Jemima studied Cellular and Molecular Medicine at the University of Bristol, UK, and as a member of the Editorial team, she now plays an integral role in shaping the content on SelectScience.
</blockquote>

SelectScience: Method development for solid phase extraction with steroid analytes

Method development for solid phase extraction with steroid analytes

We will explain the foundation of SPE and offer method development insight to a frequently tested clinical application.

Method development solid phase extraction steroid analytes

This webinar will present data and discuss EPA Draft Method 1633 compliant options to simplify sample clean up and increase sample throughput for PFAS analysis.
Key Learning Points:
<ul>
<li>Learn options for SPE phases for PFAS extraction from water and soil samples.</li>
<li>Utilize acceptable options for EPA 1633 as a guidance method.</li>
<li>Understand how to optimize time and cost for sample preparation.</li>
</ul>
<blockquote>
Presenter: Philip Bassignani (Director of Technical Operations with Alpha Analytical)
</blockquote>
<blockquote>
He has over 25 years of environmental analytical and method development experience, working on a wide range of projects. Philip serves as the laboratory’s emerging contaminants and HRMS technical specialist, with a strong emphasis on PFAS extraction and analytical method development.
</blockquote>
<blockquote>
Presenter: Richard Jack (Global Market Development Manager, Food and Environmental, Phenomenex)
</blockquote>

Phenomenex: Optimizing PFAS Analysis for Draft Method 1633 Using a Stacked SPE Format

Optimizing PFAS Analysis for Draft Method 1633 Using a Stacked SPE Format

We will present data and discuss EPA Draft Method 1633 compliant options  to simplify sample clean up and increase sample throughput for PFAS analysis.

PFAS Analysis for Draft Method 1633 Using a Stacked SPE

Welcome to the &quot;Ultra-Fast Bites&quot; series - where you can get ultra-fast insights about the latest trends and hottest topics in bite-sized content to stay at the forefront of science.
In our previous For the Love of Food! series, we have previously discussed the use of LC-GC-FID, which is the industry standard for monitoring mineral oil pollutants in edible oils and food contact materials.
These pollutants are frequently encountered as saturated (MOSH) and aromatic hydrocarbons (MOAH), making it essential to analyze for food safety. However, with the analytical challenges, additional sample clean-up procedures (AlOx and Epox) must be used to improve the method&#39;s robustness and sensitivity.
In this presentation, join us as Dr. Andreas, Managing Director of Axel Semrau GmbH &amp; Co KG, introduces a fast and efficient analysis of MOSH/MOAH using a new automated saponification workflow that can save your time and effort while maximizing the results.
For the love of food!
Learning Objectives:
<ul>
<li>Learn more about LC-GC-FID, which is the standard instrumentation to monitor the levels of MOSH/MOAH</li>
<li>Understand automated clean-up techniques for the analysis of MOSH/MOAH samples</li>
<li>Discover how the new automated saponification workflow can help save your time and effort in analysis</li>
</ul>
<blockquote>
Presenter: Dr Andreas Bruchmann (Managing Director, Axel Semrau GmbH &amp; Co KG)
</blockquote>
<blockquote>
After studying Analytical Chemistry at the University of Bochum, Andreas Bruchmann joined Axel Semrau in 1992. He worked in different departments before becoming Managing Director in 2010. Now he is responsible for the Chromatography business unit, which supplies automated application solutions for the food and pharmaceutical industry worldwide. He was also involved in the development of the CHRONECT MOSH/MOAH Workstation from the beginning in 2010.
</blockquote>

Shimadzu Corporation: Ultra-Fast Bites - For the Love of Food! Latest Update on the Analysis of MOSH/MOAH Contamination

Latest Update on the Analysis of MOSH/MOAH Contamination

A fast and efficient analysis of MOSH/MOAH using a new automated saponification workflow that can save your time and effort while maximizing the results.

The solubility of orally administered drugs is highly influenced by the composition of the intestinal fluids, the presence of fatty acids and cholesterol, and the pH. All these factors can be affected by the individual’s diet (food effect). Typical biorelevant studies, however, fail to capture food effects as the experiments are commonly performed on fixed simulated intestinal fluid (SIF) compositions. Consequently, accurate prediction of the food effect observed in clinical studies is hindered due to lack of reliable data for the model.Here, we propose a high-throughput automated workflow for the study of API solubility in complex, ad hoc biorelevant media, and the implementation of the data obtained in vitro into a Physiologically Based Biopharmaceutic Model (PBBM) used to predict the food effect on a BCS IV zwitterionic drug. The automated workflow led to considerable time and material savings, while the model accurately predicted the results of the food effect.Key Learning Objectives:<ul><li>Determination of food effect, through use of complex biorelevant media, to describe and predict clinical data</li><li>Automated preparation of ad hoc complex biorelevant media</li><li>Automated in vitro biorelevant solubility screen of an API</li><li>Integration of in vitro solubility and permeability into a Physiologically</li><li>Based Biopharmaceutic Model (PBBM)</li></ul>Who Should Attend:<ul><li>Scientist, Sr. Scientist, Development Chemist, Formulation Chemist, Process Chemist, (Directors of preceding), Research Fellow, Professor</li><li>Product Development Scientists, Biochemist</li></ul><blockquote>Presenter:&nbsp;Paola Ferrini (Investigator, High-Throughput Automation Team, GSK)Presenter: Konstantinos Stamatopoulos (Biopharmaceutics Investigator, GSK)Presenter: Catherine Dold (Health &amp; Environment Writer, C&amp;EN Media Group)</blockquote>

C&EN: Automated In Vitro Sample Preparation for PBBM to Predict Food Effect on Oral Drugs

Automated In Vitro Sample Preparation for PBBM to Predict Food Effect on Oral Drugs

We propose a high-throughput automated workflow for the study of API solubility in complex, ad hoc biorelevant media.

LCMS webinars focusing on Sample prep - page 23